Editing Prosthetic group (section)

== List of prosthetic groups ==
The table below contains a list of some of the most common prosthetic groups.
{| class="wikitable"
! Prosthetic group || Function || Distribution
 |- 
 | [[Flavin mononucleotide]]&nbsp;<ref name="Joosten">{{cite journal |author=Joosten V, van Berkel WJ |title=Flavoenzymes |journal=Curr Opin Chem Biol |volume=11 |issue=2 |pages=195–202 |year=2007 |pmid=17275397 |doi=10.1016/j.cbpa.2007.01.010}}</ref> || [[Redox]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
 |- 
 | [[FAD|Flavin adenine dinucleotide]]&nbsp;<ref name="Joosten" /> || [[Redox]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
 |-
 |[[Pyrroloquinoline quinone]]&nbsp;<ref>{{cite journal | author = Salisbury SA, Forrest HS, Cruse WB, Kennard O | title = A novel coenzyme from bacterial primary alcohol dehydrogenases | journal = Nature | year = 1979 | volume = 280 | issue = 5725 | pages = 843–4 | doi = 10.1038/280843a0| pmid = 471057 | bibcode = 1979Natur.280..843S | s2cid = 3094647 }} {{PMID|471057}}</ref> || [[Redox]] reactions || [[Bacteria]]
 |-
 |[[Pyridoxal phosphate]]&nbsp;<ref>{{cite journal |author=Eliot AC, Kirsch JF |title=Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations |journal=Annu. Rev. Biochem. |volume=73 |pages=383–415 |year=2004 |pmid=15189147 |doi=10.1146/annurev.biochem.73.011303.074021}}</ref> || [[Transamination]], [[decarboxylation]] and [[deamination]] || [[Bacteria]], [[archaea]] and [[eukaryote]]s
 |-
 |[[Biotin]]&nbsp;<ref>{{cite journal |author=Jitrapakdee S, Wallace JC |title=The biotin enzyme family: conserved structural motifs and domain rearrangements |journal=Curr. Protein Pept. Sci. |volume=4 |issue=3 |pages=217–29 |year=2003 |pmid=12769720 |doi=10.2174/1389203033487199}}</ref> || [[Carboxylation]] || [[Bacteria]], [[archaea]] and [[eukaryote]]s
 |-
 | [[Methylcobalamin]]&nbsp;<ref>{{cite journal |author=Banerjee R, Ragsdale SW |title=The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes |journal=Annu. Rev. Biochem. |volume=72 |pages=209–47 |year=2003 |pmid=14527323 |doi=10.1146/annurev.biochem.72.121801.161828|s2cid=37393683 |url=https://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1458&context=biochemfacpub |url-access=subscription }}</ref> || [[Methylation]] and [[isomerisation]] || [[Bacteria]], [[archaea]] and [[eukaryote]]s
 |- 
 |[[Thiamine pyrophosphate]]&nbsp;<ref>{{cite journal |author=Frank RA, Leeper FJ, Luisi BF |title=Structure, mechanism and catalytic duality of thiamine-dependent enzymes |journal=Cell. Mol. Life Sci. |volume=64 |issue=7–8 |pages=892–905 |year=2007 |pmid=17429582 |doi=10.1007/s00018-007-6423-5|s2cid=20415735 |pmc=11136255 }}</ref> || Transfer of 2-carbon groups, α cleavage || [[Bacteria]], [[archaea]] and [[eukaryote]]s
 |- 
 |[[Heme]]&nbsp;<ref>{{cite journal |author=Wijayanti N, Katz N, Immenschuh S |title=Biology of heme in health and disease |journal=Curr. Med. Chem. |volume=11 |issue=8 |pages=981–6 |year=2004 |pmid=15078160 |doi=10.2174/0929867043455521}}</ref> || [[Oxygen]] binding and [[redox]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
 |- 
 |[[Molybdopterin]]&nbsp;<ref>{{cite journal |author=Mendel RR, Hänsch R |title=Molybdoenzymes and molybdenum cofactor in plants |journal=J. Exp. Bot. |volume=53 |issue=375 |pages=1689–98 |year=2002 |pmid=12147719 |doi=10.1093/jxb/erf038|doi-access=free }}</ref><ref>{{cite journal |author=Mendel RR, Bittner F |title=Cell biology of molybdenum |journal=Biochim. Biophys. Acta |volume=1763 |issue=7 |pages=621–35 |year=2006 |pmid=16784786 |doi=10.1016/j.bbamcr.2006.03.013|doi-access= }}</ref> || [[Oxygenase|Oxygenation]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
 |-
 |[[Lipoic acid]]&nbsp;<ref>{{cite journal |author=Bustamante J, Lodge JK, Marcocci L, Tritschler HJ, Packer L, Rihn BH |title=Alpha-lipoic acid in liver metabolism and disease |journal=Free Radic. Biol. Med. |volume=24 |issue=6 |pages=1023–39 |year=1998 |pmid=9607614 |doi=10.1016/S0891-5849(97)00371-7}}</ref> || [[Redox]] reactions || [[Bacteria]], [[archaea]] and [[eukaryote]]s
|-
|[[Cofactor F430]]
|[[Methanogenesis]]
|[[Archaea]]
|}